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METAP2 (Methionine aminopeptidase 2)
FEATURES
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FAMILY
DESCRIPTION
Also known as MAP2_HUMAN, METAP2, MNPEP, P67EIF2. Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo., Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. Interacts strongly with the eIF-2 gamma-subunit EIF2S3 (By similarity). Binds EIF2S1 at low magnesium concentrations.
Also known as MAP2_HUMAN, METAP2, MNPEP, P67EIF2. Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is ...
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METAP2

Methionine aminopeptidase 2

Structural Ligandability

Domains Chains

Distribution